A0A1V8RU10 · A0A1V8RU10_9HYPH

  • Protein
    ATP-dependent Clp protease proteolytic subunit
  • Gene
    clpP
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
    EC:3.4.21.92 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

121120406080100120140160180200
TypeIDPosition(s)Description
Active site106Nucleophile
Active site131

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP-dependent peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent Clp protease proteolytic subunit
  • EC number
  • Alternative names
    • Endopeptidase Clp

Gene names

    • Name
      clpP
    • ORF names
      BFN67_13700

Organism names

  • Taxonomic identifier
  • Strain
    • JH-7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Pseudaminobacter

Accessions

  • Primary accession
    A0A1V8RU10

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the peptidase S14 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    211
  • Mass (Da)
    23,496
  • Last updated
    2017-06-07 v1
  • Checksum
    01BD2B8036A6BC4D
MKDPVETYMNLVPMVVEQTNRGERAYDIFSRLLKERIIFITGPIEDGMASLVCAQLLFLEAENPKKEINMYINSPGGVVTSGLAMYDTMQFIKPPVSTLCVGQAMSAGSLLLTAGAKDMRFCTPNAQIMIHQPSGGYQGQATDIMIHAQFTERLKKRLNEIYVKHTGQDYETIHNAMERDNFLTTEQALELGLIDKVLTSRDEIEAAGKEG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MDET01000006
EMBL· GenBank· DDBJ
OQM76690.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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